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- Currently displaying 1281 - 1300 of 2523 publications
Nanoscopic insights into seeding mechanisms and toxicity of α-synuclein species in neurons.
Proc Natl Acad Sci U S A
(2016)
113
3815
(doi: 10.1073/pnas.1516546113)
Ca2+ is a key factor in α-synuclein-induced neurotoxicity
J Cell Sci
(2016)
129
1792
(doi: 10.1242/jcs.180737)
Quantitative thermophoretic study of disease-related protein aggregates.
Scientific reports
(2016)
6
22829
(doi: 10.1038/srep22829)
Microfluidic Diffusion Viscometer for Rapid Analysis of Complex Solutions.
Analytical Chemistry
(2016)
88
3488
(doi: 10.1021/acs.analchem.5b02930)
Amyloid-β and α-Synuclein Decrease the Level of Metal-Catalyzed Reactive Oxygen Species by Radical Scavenging and Redox Silencing.
J Am Chem Soc
(2016)
138
3966
(doi: 10.1021/jacs.5b13577)
An Environmentally Sensitive Fluorescent Dye as a Multidimensional Probe of Amyloid Formation
The journal of physical chemistry. B
(2016)
120
2087
(doi: 10.1021/acs.jpcb.5b09663)
Alpha-Synuclein Oligomers Interact with Metal Ions to Induce Oxidative Stress and Neuronal Death in Parkinson's Disease
Antioxidants & Redox Signaling
(2016)
24
376
(doi: 10.1089/ars.2015.6343)
A structural ensemble of a ribosome-nascent chain complex during cotranslational protein folding.
Nature Structural & Molecular Biology
(2016)
23
278
(doi: 10.1038/nsmb.3182)
A Fragment-Based Method of Creating Small-Molecule Libraries to Target the Aggregation of Intrinsically Disordered Proteins.
ACS Combinatorial Science
(2016)
18
144
(doi: 10.1021/acscombsci.5b00129)
Oligomers of Heat-Shock Proteins: Structures That Don't Imply Function
Plos Computational Biology
(2016)
12
e1004756
(doi: 10.1371/journal.pcbi.1004756)
Molecular Recognition by Templated Folding of an Intrinsically Disordered Protein
Scientific Reports
(2016)
6
21994
(doi: 10.1038/srep21994)
Kinetic model of the aggregation of alpha-synuclein provides insights into prion-like spreading.
Proceedings of the National Academy of Sciences of the United States of America
(2016)
113
E1206
(doi: 10.1073/pnas.1524128113)
Structural Studies of the Oligomerization Process of Human Cystatin C Variants
Biophysical Journal
(2016)
110
26A
(doi: 10.1016/j.bpj.2015.11.205)
Consistent Treatment of Hydrophobicity in Protein Lattice Models Accounts for Cold Denaturation.
Physical Review Letters
(2016)
116
078101
Combining Single-Molecule Techniques with Microfluidics for Protein Analysis
Biophysical Journal
(2016)
110
195A
(doi: 10.1016/j.bpj.2015.11.1086)
Construction of homogeneous antibody-drug conjugates using site-selective protein chemistry.
Chem Sci
(2016)
7
2954
(doi: 10.1039/c6sc00170j)
Oligomers of heat-shock proteins: Structures that don't imply function
(2016)
(doi: 10.48550/arxiv.1508.07924)
Neuroscience: An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic Ab42 aggregates linked with Alzheimer's disease
Science advances
(2016)
2
e1501244
(doi: 10.1126/sciadv.1501244)
Automated Ex Situ Assays of Amyloid Formation on a Microfluidic Platform.
Biophys J
(2016)
110
555
(doi: 10.1016/j.bpj.2015.11.3523)
Single-Molecule Imaging of Individual Amyloid Protein Aggregates in Human Biofluids.
ACS Chem Neurosci
(2016)
7
399
(doi: 10.1021/acschemneuro.5b00324)